IF5_DROME - dbPTM
IF5_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF5_DROME
UniProt AC Q9VXK6
Protein Name Eukaryotic translation initiation factor 5
Gene Name eIF5
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 464
Subcellular Localization
Protein Description Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]) (By similarity)..
Protein Sequence MATVNVNRSVTDIFYRYKMPRLQAKVEGKGNGIKTVLVNMAEVARAIGRPATYPTKYFGCELGAQTLFDHKNERFVVNGSHDVNKLQDLLDGFIRKFVLCPECDNPETNLTVSAKNQTISQSCKACGFHGLLKVNHKVNTFIVKNPPSLNPAAQGSSLTEGKRSRKQKQKNDNADGSMTNNSLANNSGGESDGGNGTNQASQTEAEISAAIPEKTAKDDDDEGWSVDVSKEAIRARLQDLTDGAKGMTISDDYDKTEKERIDIFYELVKDKRDKKQLDDVQTHKELVIEAERLDIINKAPLVLAELLFTENIIKDVQKNRPLLLRFTLNNPKAQRYLIGGVEQTVELHKGILMSKVAGIFKLFYDLDILDEAVILEWAQKVSKRHVSKNIAAEIHEKAMPFVLWLKNAEEESSESEEEEDDESEEDNYVSSAGQRGGQRVVQRGIPRAVAGDEDDEDDVNIDDI
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
9PhosphorylationATVNVNRSVTDIFYR
CEEECCCHHHHHHHH
24.9419429919
11PhosphorylationVNVNRSVTDIFYRYK
EECCCHHHHHHHHHH
25.3219429919
156PhosphorylationLNPAAQGSSLTEGKR
CCCCCCCCCCCHHHH
15.3019429919
157PhosphorylationNPAAQGSSLTEGKRS
CCCCCCCCCCHHHHH
46.2519429919
159PhosphorylationAAQGSSLTEGKRSRK
CCCCCCCCHHHHHHH
44.6419429919
187PhosphorylationNNSLANNSGGESDGG
CCHHCCCCCCCCCCC
48.2422817900
191PhosphorylationANNSGGESDGGNGTN
CCCCCCCCCCCCCCC
44.8419060867
197PhosphorylationESDGGNGTNQASQTE
CCCCCCCCCCCHHHH
28.3229892262
201PhosphorylationGNGTNQASQTEAEIS
CCCCCCCHHHHHHHH
28.0621082442
203PhosphorylationGTNQASQTEAEISAA
CCCCCHHHHHHHHHH
34.3721082442
250PhosphorylationGAKGMTISDDYDKTE
CCCCCCCCCCCCCHH
18.4419429919
253PhosphorylationGMTISDDYDKTEKER
CCCCCCCCCCHHHHH
25.0819429919
412PhosphorylationLKNAEEESSESEEEE
ECCCCHHCCCCCCCC
42.5619429919
413PhosphorylationKNAEEESSESEEEED
CCCCHHCCCCCCCCC
48.7119429919
415PhosphorylationAEEESSESEEEEDDE
CCHHCCCCCCCCCCC
52.8619429919
423PhosphorylationEEEEDDESEEDNYVS
CCCCCCCCHHHHCHH
53.9619429919

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of IF5_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF5_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of IF5_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF2B_DROMEeIF-2betaphysical
17409115

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IF5_DROME

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-412; SER-413 ANDSER-415, AND MASS SPECTROMETRY.

TOP